A0A2A4Q357 · A0A2A4Q357_9BACT

Function

function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site.

144450100150200250300350400
TypeIDPosition(s)Description
Binding site211ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processglutamyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate--tRNA ligase
  • EC number
  • Alternative names
    • Glutamyl-tRNA synthetase
      (GluRS
      )

Gene names

    • Name
      gltX
    • ORF names
      COB80_02655

Organism names

Accessions

  • Primary accession
    A0A2A4Q357

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for motif, domain.

TypeIDPosition(s)Description
Motif11-21'HIGH' region
Domain104-276Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic
Motif208-212'KMSKS' region
Domain319-440Aminoacyl-tRNA synthetase class I anticodon-binding

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    444
  • Mass (Da)
    50,931
  • Last updated
    2017-12-20 v1
  • Checksum
    3E6D62153E43164A
MTNKIITRFPPSPTGKLHIGNIRTLLFNYLFARKNEGEVVMRFEDTDRERSSKEHEDVALETLEALGLDYDQGPFRQSERTERYVEAITKMIEDDTAYVAEESEGEKGANVIRFRNPNKEITFTDAVRGEITIDTTDFGDFVIARSKTNPIYHLTVVVDDIDMGITHVIRGEDHITSTPRQILLIEALGGTVPSYAHLPLIIGSDKKKLSKRHGAVTYQEFEELGYIPAGVLNYLALLGWNPGDEREFFTKEELIKEFSLERVNNSPAAFSYEKFDSINRHHILELXTDEYEAYVKKFLEKSDRGADLXAHHXFSEIVQQVIRERIHKFSDVTTMLEEGEFDWLLATPKPAAEDIIWKETXPETIAKHLKYVQETLENASKWSPEDLKELLWPYADENGRGEVLWPMRFSLTGAKKSPDPFMVAYLLGKEVTLERLNQAILLLE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NVSE01000024
EMBL· GenBank· DDBJ
PCH91389.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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